YTHDF3: A Potential Drug Target and Biomarker for N6-Methyladenosine RNA Binding Protein

Target Name: YTHDF3

NCBI ID: G253943

YTHDF3

YTHDF3: A Potential Drug Target and Biomarker for N6-Methyladenosine RNA Binding Protein

Introduction

YTHDF3 (YTH N6-methyladenosine RNA binding protein 3) is a protein that has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and mental disorders. Its unique function as an RNA binding protein makes it an attractive target for small molecules and other therapeutic agents that can modulate its activity. In this article, we will provide an overview of YTHDF3, its potential drug target status, and its potential as a biomarker for various diseases.

Overview of YTHDF3

YTHDF3 is a 21-kDa protein that is expressed in various tissues and cells in the human body. It is a member of the NAD+-dependent RNA binding proteins (RBP) family 3, which includes proteins that play a crucial role in regulating gene expression and translation. YTHDF3 is characterized by its unique N6-methylated adenine residue, which is located on the 2'-end of its RNA binding domain.

YTHDF3 functions as an RNA binding protein by interacting with specific target mRNAs. It has been shown to interact with various mRNAs involved in various cellular processes, including cell growth, apoptosis, and inflammation. YTHDF3 has also been shown to play a role in regulating cellular processes such as cell cycle progression, cell adhesion, and neurotransmitter release.

Potential Drug Target Status

YTHDF3's unique function as an RNA binding protein makes it an attractive target for small molecules and other therapeutic agents that can modulate its activity. Several studies have shown that YTHDF3 can be targeted by small molecules, including inhibitors of RNA binding, stabilizers of RNA, and modulators of its activity.

One of the most promising strategies for targeting YTHDF3 is the use of small molecules that can inhibit its N6-methylation activity. N6-methylation is a post-transcriptional modification that can modulate the stability and translation efficiency of mRNAs. has been shown to play a role in its stability and translation efficiency, and inhibitors of N6-methylation have been shown to be effective in modulating its activity.

In addition to inhibitors of N6-methylation, YTHDF3 can also be targeted by other small molecules that modify its activity. For example, inhibitors of RNA binding or stabilizers of RNA can also be used to modulate YTHDF3's activity. These small molecules can interact with specific residues on YTHDF3, leading to changes in its stability or translation efficiency.

Potential Biomarker Status

YTHDF3 has also been identified as a potential biomarker for various diseases. Its unique function as an RNA binding protein makes it an attractive target for diagnostic tools that can detect changes in its expression or activity.

Studies have shown that YTHDF3 is expressed in various tissues and cells involved in the development and progression of various diseases, including cancer, neurodegenerative diseases, and mental disorders. Its expression has also been associated with various diseases, including neuropathy, Alzheimer's disease, and depression.

In addition to its association with diseases, YTHDF3 has also been shown to be involved in the regulation of cellular processes that are relevant to disease progression. For example, YTHDF3 has been shown to play a role in the regulation of cell cycle progression, which is involved in the development of cancer. It has also been shown to play a role in the regulation of neurotransmitter release, which is involved in the development of neurodegenerative diseases.

Conclusion

In conclusion, YTHDF3 is a protein that has been identified as a potential drug target and biomarker for various diseases. Its unique function as an RNA binding protein makes it an attractive target for small molecules and other therapeutic agents that can modulate its activity. Its potential as a drug target and biomarker is further supported by its association with diseases and its involvement in the regulation of cellular processes that are relevant to disease progression. Further research is needed to fully understand the potential of YTHDF3 as a drug target and biomarker for various diseases .

Protein Name: YTH N6-methyladenosine RNA Binding Protein 3

Functions: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed:28106072, PubMed:28106076, PubMed:28281539, PubMed:32492408). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:22575960, PubMed:24284625, PubMed:28106072, PubMed:28281539, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3 (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:28106076, PubMed:32492408). Acts as a negative regulator of type I interferon response by down-regulating interferon-stimulated genes (ISGs) expression: acts by binding to FOXO3 mRNAs (By similarity). Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification (By similarity). Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation (PubMed:28106072). Recognizes and binds m6A-containing circular RNAs (circRNAs); circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons (PubMed:28281539). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31388144, PubMed:31292544, PubMed:32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544). May also recognize and bind N1-methyladenosine (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation (PubMed:32194978)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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